1.3.7.12: red chlorophyll catabolite reductase
This is an abbreviated version!
For detailed information about red chlorophyll catabolite reductase, go to the full flat file.
Word Map on EC 1.3.7.12
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1.3.7.12
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oxygenase
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pheophorbide
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pao
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macrocycle
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porphyrin
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pheide
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chlorophyllase
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colorless
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pheophytinase
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phototoxic
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nonfluorescent
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light-dependent
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ferredoxin-dependent
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dark-induced
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stay-green
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bilin
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degreening
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chl-binding
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postharvest
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agriculture
- 1.3.7.12
- oxygenase
- pheophorbide
- pao
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macrocycle
- porphyrin
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pheide
- chlorophyllase
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colorless
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pheophytinase
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phototoxic
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nonfluorescent
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light-dependent
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ferredoxin-dependent
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dark-induced
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stay-green
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bilin
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degreening
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chl-binding
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postharvest
- agriculture
Reaction
Synonyms
ACD2 protein, At-RCCR, AtRCCR, BoRCCR, BrRCCR, CaRCCR, EC 1.3.1.80, HvRCCR, PHAVU_008G280300g, RCC reductase, RCCR, RCCR-1, RCCR-2, red Chl catabolite reductase, red chlorophyll catabolite reductase, red-chlorophyll-catabolite reductase
ECTree
1.3.7.12 red chlorophyll catabolite reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.7.12 - red chlorophyll catabolite reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
V218V
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mutation changes the specificity of the protein from pFCC-1 (C1 isomers of pFCC) to pFCC-2 (C1 isomers of pFCC) production
F218V
additional information
F218V
mutation switches At-RCCR stereospecificity from pFCC-1 to pFCC-2 production
F218V
a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position, the F218V mutation changes the stereospecificity in RCCR. Construction of wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49
F218V
the AtRCCR mutant protein produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position. The RCC in F218V AtRCCR rotates slightly compared with that in wild-type to fill in the space generated by the substitution of Phe218 with valine. Concomitantly, the two carboxy groups of Glu154 and Asp291 move slightly away from the C20/C1 double bond. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to wild-type structures, overview
additional information
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chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
additional information
chimeric RCCRs are produced in Escherichia coli by replacing parts of mature enzyme from Arabidopsis thaliana with the respective sequences from Lycopersicon esculentum. A reversal of specificity is found in protein M, in which a domain of 37 amino acids of At-RCCR have been replaced with the respective Le-RCCR domain
additional information
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chimeric RCCRs are produced in Escherichia coli by replacing parts of mature enzyme from Arabidopsis thaliana with the respective sequences from Lycopersicon esculentum. A reversal of specificity is found in protein M, in which a domain of 37 amino acids of At-RCCR have been replaced with the respective Le-RCCR domain
additional information
construction of chimeric enzymes composed of portions of the Arabidopsis and the tomato proteins and expression in Escherichia coli, functional complementation of Arabidopsis acd2-2 mutant
additional information
construction of N-terminally truncated variants of wild-type enzyme and enzyme mutant F218V, i.e. AtRCCRDELTA49 and F218V AtRCCRDELTA49
additional information
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construction of N-terminally truncated variants of wild-type enzyme and enzyme mutant F218V, i.e. AtRCCRDELTA49 and F218V AtRCCRDELTA49
additional information
in the homologous system with both components from barley leaves, the slightly more polar pFCC-1 is produced, whereas the combination of barley membranes with soluble protein from spinach yields the less polar pFCC-2
additional information
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introduction of the stay-green gene from Festuca pratensis enzyme activity related to chlorophyll catabolism are analyzed in senescing leaves of wild-type Lolium temulentum and compared with mutant stay line leaves. During senescence of wild-type leaves chlorophylls a and b are continuously catabolised to colourless products and no other derivatives are observed, whereas in mutant stay-green leaves there is an accumulation of dephytylated and oxidised catabolites including chlorophyllide a, phaeophorbide a and 132 OH-chlorophyllide a. Pigment analysis, overview. The stay-green phenotype is not due to a mutation in RCCR in Lolium temulentum
additional information
two green pod mutant lines (M693 and M756) and one mutant line (M729) whose pod color is segregated (yellow pod named M729Y and green pod named M729G) are selected. During pod development, the genes for chlorophyll synthesis, e.g. as HEMC (Phvul.002G034500), glutamyl transfer RNA (tRNA) reductase (HEMA, Phvul.002G216100), CHLI (Phvul.003G057600, Phvul.006G178400), and POR (Phvul.005G083700, Phvul.011G148900), are decreasing throughout in the wild-type, whereas the genes for chlorophyll synthesis in the green pod mutant increased slightly from GP-2 to GP-5 and thereafter decreased. In particular, the transcription of POR (Phvul.005G083700) shows the opposite pattern when the pods extend from 2 to 5 cm, which is increased in the green pod mutant but decreased steeply in wild-type
additional information
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chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
additional information
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in the homologous system with both components from barley leaves, the slightly more polar pFCC-1 is produced, whereas the combination of barley membranes with soluble protein from spinach yields the less polar pFCC-2
